A novel ATP dependent dimethylsulfoniopropionate lyase in bacteria that releases dimethyl sulfide and acryloyl-CoA

Dimethylsulfoniopropionate (DMSP) is an abundant and ubiquitous organosulfur molecule in marine environments with important roles in global sulfur and nutrient cycling. Diverse DMSP lyases in some algae, bacteria, and fungi cleave DMSP to yield gaseous dimethyl sulfide (DMS), an infochemical with im...

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Autores principales: Chun-Yang Li, Xiu-Juan Wang, Xiu-Lan Chen, Qi Sheng, Shan Zhang, Peng Wang, Mussa Quareshy, Branko Rihtman, Xuan Shao, Chao Gao, Fuchuan Li, Shengying Li, Weipeng Zhang, Xiao-Hua Zhang, Gui-Peng Yang, Jonathan D Todd, Yin Chen, Yu-Zhong Zhang
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Publicado: eLife Sciences Publications Ltd 2021
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spelling oai:doaj.org-article:155c9dc9f49743a7b384a5b4174ce9402021-11-25T14:34:59ZA novel ATP dependent dimethylsulfoniopropionate lyase in bacteria that releases dimethyl sulfide and acryloyl-CoA10.7554/eLife.640452050-084Xe64045https://doaj.org/article/155c9dc9f49743a7b384a5b4174ce9402021-05-01T00:00:00Zhttps://elifesciences.org/articles/64045https://doaj.org/toc/2050-084XDimethylsulfoniopropionate (DMSP) is an abundant and ubiquitous organosulfur molecule in marine environments with important roles in global sulfur and nutrient cycling. Diverse DMSP lyases in some algae, bacteria, and fungi cleave DMSP to yield gaseous dimethyl sulfide (DMS), an infochemical with important roles in atmospheric chemistry. Here, we identified a novel ATP-dependent DMSP lyase, DddX. DddX belongs to the acyl-CoA synthetase superfamily and is distinct from the eight other known DMSP lyases. DddX catalyses the conversion of DMSP to DMS via a two-step reaction: the ligation of DMSP with CoA to form the intermediate DMSP-CoA, which is then cleaved to DMS and acryloyl-CoA. The novel catalytic mechanism was elucidated by structural and biochemical analyses. DddX is found in several Alphaproteobacteria, Gammaproteobacteria, and Firmicutes, suggesting that this new DMSP lyase may play an overlooked role in DMSP/DMS cycles.Chun-Yang LiXiu-Juan WangXiu-Lan ChenQi ShengShan ZhangPeng WangMussa QuareshyBranko RihtmanXuan ShaoChao GaoFuchuan LiShengying LiWeipeng ZhangXiao-Hua ZhangGui-Peng YangJonathan D ToddYin ChenYu-Zhong ZhangeLife Sciences Publications Ltdarticledmsp cleavage pathwaydms generationATP-dependent DMSP lyaseglobal sulfur cyclemarine bacteriaMedicineRScienceQBiology (General)QH301-705.5ENeLife, Vol 10 (2021)
institution DOAJ
collection DOAJ
language EN
topic dmsp cleavage pathway
dms generation
ATP-dependent DMSP lyase
global sulfur cycle
marine bacteria
Medicine
R
Science
Q
Biology (General)
QH301-705.5
spellingShingle dmsp cleavage pathway
dms generation
ATP-dependent DMSP lyase
global sulfur cycle
marine bacteria
Medicine
R
Science
Q
Biology (General)
QH301-705.5
Chun-Yang Li
Xiu-Juan Wang
Xiu-Lan Chen
Qi Sheng
Shan Zhang
Peng Wang
Mussa Quareshy
Branko Rihtman
Xuan Shao
Chao Gao
Fuchuan Li
Shengying Li
Weipeng Zhang
Xiao-Hua Zhang
Gui-Peng Yang
Jonathan D Todd
Yin Chen
Yu-Zhong Zhang
A novel ATP dependent dimethylsulfoniopropionate lyase in bacteria that releases dimethyl sulfide and acryloyl-CoA
description Dimethylsulfoniopropionate (DMSP) is an abundant and ubiquitous organosulfur molecule in marine environments with important roles in global sulfur and nutrient cycling. Diverse DMSP lyases in some algae, bacteria, and fungi cleave DMSP to yield gaseous dimethyl sulfide (DMS), an infochemical with important roles in atmospheric chemistry. Here, we identified a novel ATP-dependent DMSP lyase, DddX. DddX belongs to the acyl-CoA synthetase superfamily and is distinct from the eight other known DMSP lyases. DddX catalyses the conversion of DMSP to DMS via a two-step reaction: the ligation of DMSP with CoA to form the intermediate DMSP-CoA, which is then cleaved to DMS and acryloyl-CoA. The novel catalytic mechanism was elucidated by structural and biochemical analyses. DddX is found in several Alphaproteobacteria, Gammaproteobacteria, and Firmicutes, suggesting that this new DMSP lyase may play an overlooked role in DMSP/DMS cycles.
format article
author Chun-Yang Li
Xiu-Juan Wang
Xiu-Lan Chen
Qi Sheng
Shan Zhang
Peng Wang
Mussa Quareshy
Branko Rihtman
Xuan Shao
Chao Gao
Fuchuan Li
Shengying Li
Weipeng Zhang
Xiao-Hua Zhang
Gui-Peng Yang
Jonathan D Todd
Yin Chen
Yu-Zhong Zhang
author_facet Chun-Yang Li
Xiu-Juan Wang
Xiu-Lan Chen
Qi Sheng
Shan Zhang
Peng Wang
Mussa Quareshy
Branko Rihtman
Xuan Shao
Chao Gao
Fuchuan Li
Shengying Li
Weipeng Zhang
Xiao-Hua Zhang
Gui-Peng Yang
Jonathan D Todd
Yin Chen
Yu-Zhong Zhang
author_sort Chun-Yang Li
title A novel ATP dependent dimethylsulfoniopropionate lyase in bacteria that releases dimethyl sulfide and acryloyl-CoA
title_short A novel ATP dependent dimethylsulfoniopropionate lyase in bacteria that releases dimethyl sulfide and acryloyl-CoA
title_full A novel ATP dependent dimethylsulfoniopropionate lyase in bacteria that releases dimethyl sulfide and acryloyl-CoA
title_fullStr A novel ATP dependent dimethylsulfoniopropionate lyase in bacteria that releases dimethyl sulfide and acryloyl-CoA
title_full_unstemmed A novel ATP dependent dimethylsulfoniopropionate lyase in bacteria that releases dimethyl sulfide and acryloyl-CoA
title_sort novel atp dependent dimethylsulfoniopropionate lyase in bacteria that releases dimethyl sulfide and acryloyl-coa
publisher eLife Sciences Publications Ltd
publishDate 2021
url https://doaj.org/article/155c9dc9f49743a7b384a5b4174ce940
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